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Evidence for Autocatalytic Cross-Linking of Hydroxyproline-Rich Glycoproteins during Extracellular Matrix Assembly in Volvox

Lehrstuhl Biochemie I, Universität Regensburg, D-93040 Regensburg, Germany

¹ To whom correspondence should be addressed. E-mail manfred.sumper{at}vkl.uni-regensburg.de; fax 49-941-943-2936

The alga Volvox carteri is one of the simplest multicellular organisms, yet it has a surprisingly complex extracellular matrix (ECM), making Volvox suitable as a model system in which to study ECM self-assembly. Here, we analyze the primary structures and post-translational modifications of two main ECM components synthesized in response to sexual induction as well as wounding. These proteins are members of the pherophorin family with as yet unknown properties. They contain polyhydroxyproline spacers as long as 500 and 2750 residues. Even the highly purified proteins retain the capacity to self-assemble and cross-link, producing an insoluble fibrous network in an apparently autocatalytic reaction. This pherophorin-based network is located within the deep zone of the ECM. A molecular genetic search for additional members of the pherophorin family indicates that at least nine different pherophorin species can be expected to serve as precursors for ECM substructures. Therefore, the highly diversified members of the pherophorin family represent region-specific morphological building blocks for ECM assembly and cross-linking.

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